HEADER HYDROLASE 26-APR-06 2GSO
TITLE STRUCTURE OF XAC NUCLEOTIDE PYROPHOSPHATASE/PHOSPHODIESTERASE IN
TITLE 2 COMPLEX WITH VANADATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHODIESTERASE-NUCLEOTIDE PYROPHOSPHATASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES (44-425);
COMPND 5 EC: 3.6.1.9;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: XANTHOMONAS AXONOPODIS PV. CITRI STR. 306;
SOURCE 3 ORGANISM_TAXID: 190486;
SOURCE 4 STRAIN: PV. CITRI STR. 306;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ALPHA BETA, NPP, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.G.ZALATAN,T.D.FENN,A.T.BRUNGER,D.HERSCHLAG
REVDAT 4 18-OCT-17 2GSO 1 REMARK
REVDAT 3 24-FEB-09 2GSO 1 VERSN
REVDAT 2 22-AUG-06 2GSO 1 JRNL
REVDAT 1 01-AUG-06 2GSO 0
JRNL AUTH J.G.ZALATAN,T.D.FENN,A.T.BRUNGER,D.HERSCHLAG
JRNL TITL STRUCTURAL AND FUNCTIONAL COMPARISONS OF NUCLEOTIDE
JRNL TITL 2 PYROPHOSPHATASE/PHOSPHODIESTERASE AND ALKALINE PHOSPHATASE:
JRNL TITL 3 IMPLICATIONS FOR MECHANISM AND EVOLUTION
JRNL REF BIOCHEMISTRY V. 45 9788 2006
JRNL REFN ISSN 0006-2960
JRNL PMID 16893180
JRNL DOI 10.1021/BI060847T
REMARK 2
REMARK 2 RESOLUTION. 1.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.3
REMARK 3 NUMBER OF REFLECTIONS : 140234
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.193
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 7390
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.34
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2601
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 22.72
REMARK 3 BIN R VALUE (WORKING SET) : 0.4110
REMARK 3 BIN FREE R VALUE SET COUNT : 155
REMARK 3 BIN FREE R VALUE : 0.4230
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5882
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 14
REMARK 3 SOLVENT ATOMS : 847
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.57
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.05000
REMARK 3 B22 (A**2) : 0.01000
REMARK 3 B33 (A**2) : -0.06000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.059
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.059
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.041
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.080
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.973
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.967
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6240 ; 0.009 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 5567 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8554 ; 1.235 ; 1.937
REMARK 3 BOND ANGLES OTHERS (DEGREES): 12885 ; 0.806 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 806 ; 5.944 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 286 ;34.122 ;22.517
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 917 ;12.193 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 61 ;12.511 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 900 ; 0.074 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7241 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1328 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1296 ; 0.203 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 5835 ; 0.188 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3012 ; 0.174 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 3648 ; 0.081 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 617 ; 0.118 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 7 ; 0.035 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 30 ; 0.146 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 159 ; 0.254 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 71 ; 0.110 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 5033 ; 0.784 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1596 ; 0.158 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6320 ; 0.901 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2677 ; 1.463 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2234 ; 2.177 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 8 ; 2.874 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 4 ; 1.869 ; 3.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 10 ; 7.216 ; 3.000
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 44 A 425 4
REMARK 3 1 B 44 B 425 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 5665 ; 0.24 ; 0.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 5665 ; 0.61 ; 2.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 44 A 425
REMARK 3 ORIGIN FOR THE GROUP (A): 24.0551 39.8826 27.1051
REMARK 3 T TENSOR
REMARK 3 T11: -0.0275 T22: -0.0135
REMARK 3 T33: -0.0097 T12: -0.0022
REMARK 3 T13: -0.0012 T23: -0.0032
REMARK 3 L TENSOR
REMARK 3 L11: 0.5161 L22: 0.1487
REMARK 3 L33: 0.2552 L12: 0.1090
REMARK 3 L13: 0.0669 L23: -0.0146
REMARK 3 S TENSOR
REMARK 3 S11: -0.0226 S12: 0.0229 S13: 0.0148
REMARK 3 S21: 0.0069 S22: 0.0147 S23: 0.0157
REMARK 3 S31: -0.0033 S32: 0.0010 S33: 0.0079
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 44 B 425
REMARK 3 ORIGIN FOR THE GROUP (A): 41.4270 39.1364 60.4759
REMARK 3 T TENSOR
REMARK 3 T11: 0.0223 T22: -0.0344
REMARK 3 T33: -0.0146 T12: 0.0036
REMARK 3 T13: 0.0050 T23: 0.0075
REMARK 3 L TENSOR
REMARK 3 L11: 0.4588 L22: 0.1310
REMARK 3 L33: 0.1067 L12: -0.0985
REMARK 3 L13: -0.0810 L23: 0.0699
REMARK 3 S TENSOR
REMARK 3 S11: -0.0563 S12: 0.0022 S13: -0.0096
REMARK 3 S21: 0.0264 S22: 0.0280 S23: -0.0063
REMARK 3 S31: 0.0290 S32: -0.0005 S33: 0.0283
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2GSO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-MAY-06.
REMARK 100 THE DEPOSITION ID IS D_1000037505.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-NOV-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9537
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL, SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : BOS
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 147720
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.300
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.08500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.35
REMARK 200 COMPLETENESS FOR SHELL (%) : 28.3
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.11
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BIS-TRIS HCL, 18% PEG 3350, PH
REMARK 280 6.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 33.02000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 64.84300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.38800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 64.84300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.02000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.38800
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: DIMER IN ASYMMETRIC UNIT, LIKELY FUNCTIONAL AS A MONOMER
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ALA A 40
REMARK 465 SER A 41
REMARK 465 ALA A 42
REMARK 465 SER A 43
REMARK 465 PRO A 426
REMARK 465 PRO A 427
REMARK 465 ALA A 428
REMARK 465 PRO A 429
REMARK 465 ASP A 430
REMARK 465 ALA A 431
REMARK 465 ARG A 432
REMARK 465 ALA B 40
REMARK 465 SER B 41
REMARK 465 ALA B 42
REMARK 465 SER B 43
REMARK 465 PRO B 426
REMARK 465 PRO B 427
REMARK 465 ALA B 428
REMARK 465 PRO B 429
REMARK 465 ASP B 430
REMARK 465 ALA B 431
REMARK 465 ARG B 432
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 155 35.63 72.93
REMARK 500 ALA A 162 72.99 -101.36
REMARK 500 ARG A 357 -63.23 -142.09
REMARK 500 HIS A 363 -152.34 -128.71
REMARK 500 ASP A 366 117.01 -38.34
REMARK 500 SER B 155 31.57 72.62
REMARK 500 ASP B 194 -167.81 -124.96
REMARK 500 ASP B 194 -167.81 -123.32
REMARK 500 HIS B 267 32.30 -99.19
REMARK 500 HIS B 311 27.90 -140.19
REMARK 500 ARG B 357 -72.65 -159.71
REMARK 500 HIS B 363 -150.32 -128.73
REMARK 500 ASP B 366 117.15 -38.58
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 VO4 A1004 V
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 90 OG1
REMARK 620 2 VO4 A1004 O1 94.2
REMARK 620 3 VO4 A1004 O2 102.4 113.2
REMARK 620 4 VO4 A1004 O3 74.7 123.0 123.8
REMARK 620 5 VO4 A1004 O4 156.8 88.4 97.8 84.5
REMARK 620 6 HOH A1431 O 83.8 169.9 58.0 66.0 97.5
REMARK 620 7 ZN A1001 ZN 113.2 103.0 126.5 42.0 44.0 86.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1000 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 90 OG1
REMARK 620 2 ASP A 257 OD2 103.3
REMARK 620 3 HIS A 258 NE2 114.8 90.6
REMARK 620 4 VO4 A1004 O3 66.5 169.5 96.1
REMARK 620 5 ASP A 54 OD1 131.8 99.0 107.1 86.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1001 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VO4 A1004 O3
REMARK 620 2 ASP A 210 OD2 73.7
REMARK 620 3 ASP A 210 OD1 81.1 56.1
REMARK 620 4 HIS A 214 NE2 159.9 88.5 96.9
REMARK 620 5 HIS A 363 NE2 95.1 154.1 99.8 104.9
REMARK 620 6 VO4 A1004 O4 76.4 100.6 151.6 98.4 99.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 VO4 B1005 V
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR B 90 OG1
REMARK 620 2 VO4 B1005 O1 88.5
REMARK 620 3 VO4 B1005 O2 103.8 113.8
REMARK 620 4 VO4 B1005 O3 79.2 121.0 125.1
REMARK 620 5 VO4 B1005 O4 157.5 91.1 96.9 81.7
REMARK 620 6 HOH B1234 O 82.8 167.7 60.4 65.9 100.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1002 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VO4 B1005 O3
REMARK 620 2 HIS B 258 NE2 95.3
REMARK 620 3 ASP B 257 OD2 170.1 91.0
REMARK 620 4 THR B 90 OG1 67.7 114.3 102.7
REMARK 620 5 ASP B 54 OD1 86.1 110.2 98.9 129.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1003 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 210 OD2
REMARK 620 2 ASP B 210 OD1 54.7
REMARK 620 3 VO4 B1005 O3 72.6 81.7
REMARK 620 4 HIS B 214 NE2 88.7 96.9 158.1
REMARK 620 5 VO4 B1005 O4 99.3 148.7 73.0 99.8
REMARK 620 6 HIS B 363 NE2 153.5 100.1 97.7 104.0 101.2
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VO4 A 1004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VO4 B 1005
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2GSN RELATED DB: PDB
REMARK 900 RELATED ID: 2GSU RELATED DB: PDB
DBREF 2GSO A 40 432 UNP Q8PIS1 Q8PIS1_XANAC 40 432
DBREF 2GSO B 40 432 UNP Q8PIS1 Q8PIS1_XANAC 40 432
SEQRES 1 A 393 ALA SER ALA SER THR PRO HIS ALA LEU LEU LEU ILE SER
SEQRES 2 A 393 ILE ASP GLY LEU ARG ALA ASP MET LEU ASP ARG GLY ILE
SEQRES 3 A 393 THR PRO ASN LEU SER HIS LEU ALA ARG GLU GLY VAL ARG
SEQRES 4 A 393 ALA ARG TRP MET ALA PRO SER TYR PRO SER LEU THR PHE
SEQRES 5 A 393 PRO ASN HIS TYR THR LEU VAL THR GLY LEU ARG PRO ASP
SEQRES 6 A 393 HIS HIS GLY ILE VAL HIS ASN SER MET ARG ASP PRO THR
SEQRES 7 A 393 LEU GLY GLY PHE TRP LEU SER LYS SER GLU ALA VAL GLY
SEQRES 8 A 393 ASP ALA ARG TRP TRP GLY GLY GLU PRO VAL TRP VAL GLY
SEQRES 9 A 393 VAL GLU ASN THR GLY GLN HIS ALA ALA THR TRP SER TRP
SEQRES 10 A 393 PRO GLY SER GLU ALA ALA ILE LYS GLY VAL ARG PRO SER
SEQRES 11 A 393 GLN TRP ARG HIS TYR GLN LYS GLY VAL ARG LEU ASP THR
SEQRES 12 A 393 ARG VAL ASP ALA VAL ARG GLY TRP LEU ALA THR ASP GLY
SEQRES 13 A 393 ALA GLN ARG ASN ARG LEU VAL THR LEU TYR PHE GLU HIS
SEQRES 14 A 393 VAL ASP GLU ALA GLY HIS ASP HIS GLY PRO GLU SER ARG
SEQRES 15 A 393 GLN TYR ALA ASP ALA VAL ARG ALA VAL ASP ALA ALA ILE
SEQRES 16 A 393 GLY ARG LEU LEU ALA GLY MET GLN ARG ASP GLY THR ARG
SEQRES 17 A 393 ALA ARG THR ASN ILE ILE VAL VAL SER ASP HIS GLY MET
SEQRES 18 A 393 ALA GLU VAL ALA PRO GLY HIS ALA ILE SER VAL GLU ASP
SEQRES 19 A 393 ILE ALA PRO PRO GLN ILE ALA THR ALA ILE THR ASP GLY
SEQRES 20 A 393 GLN VAL ILE GLY PHE GLU PRO LEU PRO GLY GLN GLN ALA
SEQRES 21 A 393 ALA ALA GLU ALA SER VAL LEU GLY ALA HIS ASP HIS TYR
SEQRES 22 A 393 ASP CYS TRP ARG LYS ALA GLU LEU PRO ALA ARG TRP GLN
SEQRES 23 A 393 TYR GLY SER HIS PRO ARG ILE PRO SER LEU VAL CYS GLN
SEQRES 24 A 393 MET HIS GLU GLY TRP ASP ALA LEU PHE PRO ASP LYS LEU
SEQRES 25 A 393 ALA LYS ARG ALA GLN ARG GLY THR ARG GLY SER HIS GLY
SEQRES 26 A 393 TYR ASP PRO ALA LEU PRO SER MET ARG ALA VAL PHE LEU
SEQRES 27 A 393 ALA GLN GLY PRO ASP LEU ALA GLN GLY LYS THR LEU PRO
SEQRES 28 A 393 GLY PHE ASP ASN VAL ASP VAL TYR ALA LEU MET SER ARG
SEQRES 29 A 393 LEU LEU GLY ILE PRO ALA ALA PRO ASN ASP GLY ASN PRO
SEQRES 30 A 393 ALA THR LEU LEU PRO ALA LEU ARG MET PRO PRO ALA PRO
SEQRES 31 A 393 ASP ALA ARG
SEQRES 1 B 393 ALA SER ALA SER THR PRO HIS ALA LEU LEU LEU ILE SER
SEQRES 2 B 393 ILE ASP GLY LEU ARG ALA ASP MET LEU ASP ARG GLY ILE
SEQRES 3 B 393 THR PRO ASN LEU SER HIS LEU ALA ARG GLU GLY VAL ARG
SEQRES 4 B 393 ALA ARG TRP MET ALA PRO SER TYR PRO SER LEU THR PHE
SEQRES 5 B 393 PRO ASN HIS TYR THR LEU VAL THR GLY LEU ARG PRO ASP
SEQRES 6 B 393 HIS HIS GLY ILE VAL HIS ASN SER MET ARG ASP PRO THR
SEQRES 7 B 393 LEU GLY GLY PHE TRP LEU SER LYS SER GLU ALA VAL GLY
SEQRES 8 B 393 ASP ALA ARG TRP TRP GLY GLY GLU PRO VAL TRP VAL GLY
SEQRES 9 B 393 VAL GLU ASN THR GLY GLN HIS ALA ALA THR TRP SER TRP
SEQRES 10 B 393 PRO GLY SER GLU ALA ALA ILE LYS GLY VAL ARG PRO SER
SEQRES 11 B 393 GLN TRP ARG HIS TYR GLN LYS GLY VAL ARG LEU ASP THR
SEQRES 12 B 393 ARG VAL ASP ALA VAL ARG GLY TRP LEU ALA THR ASP GLY
SEQRES 13 B 393 ALA GLN ARG ASN ARG LEU VAL THR LEU TYR PHE GLU HIS
SEQRES 14 B 393 VAL ASP GLU ALA GLY HIS ASP HIS GLY PRO GLU SER ARG
SEQRES 15 B 393 GLN TYR ALA ASP ALA VAL ARG ALA VAL ASP ALA ALA ILE
SEQRES 16 B 393 GLY ARG LEU LEU ALA GLY MET GLN ARG ASP GLY THR ARG
SEQRES 17 B 393 ALA ARG THR ASN ILE ILE VAL VAL SER ASP HIS GLY MET
SEQRES 18 B 393 ALA GLU VAL ALA PRO GLY HIS ALA ILE SER VAL GLU ASP
SEQRES 19 B 393 ILE ALA PRO PRO GLN ILE ALA THR ALA ILE THR ASP GLY
SEQRES 20 B 393 GLN VAL ILE GLY PHE GLU PRO LEU PRO GLY GLN GLN ALA
SEQRES 21 B 393 ALA ALA GLU ALA SER VAL LEU GLY ALA HIS ASP HIS TYR
SEQRES 22 B 393 ASP CYS TRP ARG LYS ALA GLU LEU PRO ALA ARG TRP GLN
SEQRES 23 B 393 TYR GLY SER HIS PRO ARG ILE PRO SER LEU VAL CYS GLN
SEQRES 24 B 393 MET HIS GLU GLY TRP ASP ALA LEU PHE PRO ASP LYS LEU
SEQRES 25 B 393 ALA LYS ARG ALA GLN ARG GLY THR ARG GLY SER HIS GLY
SEQRES 26 B 393 TYR ASP PRO ALA LEU PRO SER MET ARG ALA VAL PHE LEU
SEQRES 27 B 393 ALA GLN GLY PRO ASP LEU ALA GLN GLY LYS THR LEU PRO
SEQRES 28 B 393 GLY PHE ASP ASN VAL ASP VAL TYR ALA LEU MET SER ARG
SEQRES 29 B 393 LEU LEU GLY ILE PRO ALA ALA PRO ASN ASP GLY ASN PRO
SEQRES 30 B 393 ALA THR LEU LEU PRO ALA LEU ARG MET PRO PRO ALA PRO
SEQRES 31 B 393 ASP ALA ARG
HET ZN A1000 1
HET ZN A1001 1
HET VO4 A1004 5
HET ZN B1002 1
HET ZN B1003 1
HET VO4 B1005 5
HETNAM ZN ZINC ION
HETNAM VO4 VANADATE ION
FORMUL 3 ZN 4(ZN 2+)
FORMUL 5 VO4 2(O4 V 3-)
FORMUL 9 HOH *847(H2 O)
HELIX 1 1 ARG A 57 ARG A 63 5 7
HELIX 2 2 THR A 66 GLY A 76 1 11
HELIX 3 3 LEU A 89 GLY A 100 1 12
HELIX 4 4 ARG A 102 GLY A 107 1 6
HELIX 5 5 LYS A 125 GLY A 130 1 6
HELIX 6 6 ASP A 131 TRP A 135 5 5
HELIX 7 7 PRO A 139 THR A 147 1 9
HELIX 8 8 ALA A 162 VAL A 166 5 5
HELIX 9 9 ARG A 179 THR A 193 1 15
HELIX 10 10 ASP A 194 GLN A 197 5 4
HELIX 11 11 GLU A 207 GLY A 217 1 11
HELIX 12 12 SER A 220 ASP A 244 1 25
HELIX 13 13 THR A 246 ALA A 248 5 3
HELIX 14 14 GLU A 272 ILE A 274 5 3
HELIX 15 15 GLN A 297 LEU A 306 1 10
HELIX 16 16 ALA A 318 LEU A 320 5 3
HELIX 17 17 PRO A 321 GLN A 325 5 5
HELIX 18 18 PHE A 347 ARG A 354 1 8
HELIX 19 19 LEU A 369 ARG A 373 5 5
HELIX 20 20 ASP A 396 GLY A 406 1 11
HELIX 21 21 LEU A 419 LEU A 423 5 5
HELIX 22 22 ARG B 57 ASP B 62 5 6
HELIX 23 23 THR B 66 GLY B 76 1 11
HELIX 24 24 LEU B 89 GLY B 100 1 12
HELIX 25 25 ARG B 102 GLY B 107 1 6
HELIX 26 26 LYS B 125 GLY B 130 1 6
HELIX 27 27 ASP B 131 TRP B 135 5 5
HELIX 28 28 PRO B 139 THR B 147 1 9
HELIX 29 29 ALA B 162 VAL B 166 5 5
HELIX 30 30 ARG B 179 THR B 193 1 15
HELIX 31 31 ASP B 194 GLN B 197 5 4
HELIX 32 32 GLU B 207 GLY B 217 1 11
HELIX 33 33 SER B 220 ASP B 244 1 25
HELIX 34 34 THR B 246 ALA B 248 5 3
HELIX 35 35 VAL B 271 ALA B 275 1 5
HELIX 36 36 GLN B 297 LEU B 306 1 10
HELIX 37 37 ALA B 318 LEU B 320 5 3
HELIX 38 38 PRO B 321 GLN B 325 5 5
HELIX 39 39 PHE B 347 ARG B 354 1 8
HELIX 40 40 LEU B 369 ARG B 373 5 5
HELIX 41 41 ASP B 396 LEU B 405 1 10
HELIX 42 42 LEU B 419 LEU B 423 5 5
SHEET 1 A 7 HIS A 150 THR A 153 0
SHEET 2 A 7 ASN A 199 PHE A 206 1 O THR A 203 N ALA A 152
SHEET 3 A 7 ALA A 47 ILE A 53 1 N LEU A 48 O ARG A 200
SHEET 4 A 7 THR A 250 VAL A 255 1 O ASN A 251 N ALA A 47
SHEET 5 A 7 PHE A 376 GLN A 379 -1 O GLN A 379 N ILE A 252
SHEET 6 A 7 VAL A 77 ALA A 79 -1 N VAL A 77 O ALA A 378
SHEET 7 A 7 LYS A 387 LEU A 389 1 O LEU A 389 N ARG A 78
SHEET 1 B 2 MET A 82 ALA A 83 0
SHEET 2 B 2 PHE A 392 ASP A 393 1 O PHE A 392 N ALA A 83
SHEET 1 C 2 MET A 113 ASP A 115 0
SHEET 2 C 2 GLY A 119 PHE A 121 -1 O PHE A 121 N MET A 113
SHEET 1 D 2 ALA A 261 VAL A 263 0
SHEET 2 D 2 ARG A 360 SER A 362 -1 O SER A 362 N ALA A 261
SHEET 1 E 2 ALA A 268 SER A 270 0
SHEET 2 E 2 ASP A 344 LEU A 346 1 O LEU A 346 N ILE A 269
SHEET 1 F 5 ALA A 280 ALA A 282 0
SHEET 2 F 5 VAL A 288 PRO A 293 -1 O GLU A 292 N THR A 281
SHEET 3 F 5 LEU A 335 MET A 339 -1 O LEU A 335 N PHE A 291
SHEET 4 F 5 TYR A 312 ARG A 316 -1 N ASP A 313 O GLN A 338
SHEET 5 F 5 GLY A 307 ALA A 308 -1 N GLY A 307 O CYS A 314
SHEET 1 G 7 HIS B 150 THR B 153 0
SHEET 2 G 7 ASN B 199 PHE B 206 1 O LEU B 201 N ALA B 152
SHEET 3 G 7 ALA B 47 ILE B 53 1 N LEU B 48 O ARG B 200
SHEET 4 G 7 THR B 250 VAL B 255 1 O ASN B 251 N LEU B 49
SHEET 5 G 7 PHE B 376 GLN B 379 -1 O GLN B 379 N ILE B 252
SHEET 6 G 7 VAL B 77 ALA B 79 -1 N VAL B 77 O ALA B 378
SHEET 7 G 7 LYS B 387 LEU B 389 1 O LEU B 389 N ARG B 78
SHEET 1 H 2 MET B 82 ALA B 83 0
SHEET 2 H 2 PHE B 392 ASP B 393 1 O PHE B 392 N ALA B 83
SHEET 1 I 2 MET B 113 ASP B 115 0
SHEET 2 I 2 GLY B 119 PHE B 121 -1 O PHE B 121 N MET B 113
SHEET 1 J 2 ALA B 261 VAL B 263 0
SHEET 2 J 2 ARG B 360 SER B 362 -1 O ARG B 360 N VAL B 263
SHEET 1 K 2 ALA B 268 SER B 270 0
SHEET 2 K 2 ASP B 344 LEU B 346 1 O LEU B 346 N ILE B 269
SHEET 1 L 5 ALA B 280 ALA B 282 0
SHEET 2 L 5 VAL B 288 PRO B 293 -1 O GLU B 292 N THR B 281
SHEET 3 L 5 LEU B 335 MET B 339 -1 O LEU B 335 N PHE B 291
SHEET 4 L 5 TYR B 312 ARG B 316 -1 N TRP B 315 O VAL B 336
SHEET 5 L 5 GLY B 307 HIS B 309 -1 N HIS B 309 O TYR B 312
SSBOND 1 CYS A 314 CYS A 337 1555 1555 2.07
SSBOND 2 CYS B 314 CYS B 337 1555 1555 2.08
LINK OG1 THR A 90 V VO4 A1004 1555 1555 1.89
LINK ZN ZN A1000 OG1 THR A 90 1555 1555 2.08
LINK ZN ZN A1000 OD2 ASP A 257 1555 1555 2.11
LINK ZN ZN A1000 NE2 HIS A 258 1555 1555 2.04
LINK ZN ZN A1000 O3 VO4 A1004 1555 1555 2.26
LINK ZN ZN A1000 OD1 ASP A 54 1555 1555 2.05
LINK ZN ZN A1001 O3 VO4 A1004 1555 1555 2.12
LINK ZN ZN A1001 OD2 ASP A 210 1555 1555 2.47
LINK ZN ZN A1001 OD1 ASP A 210 1555 1555 2.20
LINK ZN ZN A1001 NE2 HIS A 214 1555 1555 2.04
LINK ZN ZN A1001 NE2 HIS A 363 1555 1555 2.10
LINK ZN ZN A1001 O4 VO4 A1004 1555 1555 2.20
LINK V VO4 A1004 O HOH A1431 1555 1555 3.01
LINK V VO4 A1004 ZN ZN A1001 1555 1555 3.13
LINK OG1 THR B 90 V VO4 B1005 1555 1555 1.91
LINK ZN ZN B1002 O3 VO4 B1005 1555 1555 2.30
LINK ZN ZN B1002 NE2 HIS B 258 1555 1555 2.04
LINK ZN ZN B1002 OD2 ASP B 257 1555 1555 2.10
LINK ZN ZN B1002 OG1 THR B 90 1555 1555 2.10
LINK ZN ZN B1002 OD1 ASP B 54 1555 1555 2.05
LINK ZN ZN B1003 OD2 ASP B 210 1555 1555 2.55
LINK ZN ZN B1003 OD1 ASP B 210 1555 1555 2.19
LINK ZN ZN B1003 O3 VO4 B1005 1555 1555 2.14
LINK ZN ZN B1003 NE2 HIS B 214 1555 1555 2.03
LINK ZN ZN B1003 O4 VO4 B1005 1555 1555 2.13
LINK ZN ZN B1003 NE2 HIS B 363 1555 1555 2.05
LINK V VO4 B1005 O HOH B1234 1555 1555 2.85
CISPEP 1 TYR A 86 PRO A 87 0 -2.85
CISPEP 2 TYR B 86 PRO B 87 0 -3.42
SITE 1 AC1 5 ASP A 54 THR A 90 ASP A 257 HIS A 258
SITE 2 AC1 5 VO4 A1004
SITE 1 AC2 4 ASP A 210 HIS A 214 HIS A 363 VO4 A1004
SITE 1 AC3 13 ASP A 54 THR A 90 ASN A 111 ASP A 210
SITE 2 AC3 13 HIS A 214 HIS A 258 HIS A 363 ZN A1000
SITE 3 AC3 13 ZN A1001 HOH A1033 HOH A1283 HOH A1367
SITE 4 AC3 13 HOH A1431
SITE 1 AC4 5 ASP B 54 THR B 90 ASP B 257 HIS B 258
SITE 2 AC4 5 VO4 B1005
SITE 1 AC5 4 ASP B 210 HIS B 214 HIS B 363 VO4 B1005
SITE 1 AC6 13 ASP B 54 THR B 90 ASN B 111 LEU B 123
SITE 2 AC6 13 ASP B 210 HIS B 214 HIS B 258 HIS B 363
SITE 3 AC6 13 ZN B1002 ZN B1003 HOH B1234 HOH B1292
SITE 4 AC6 13 HOH B1343
CRYST1 66.040 78.776 129.686 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.015142 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012694 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007711 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
